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Report No.

Crystallization of proteinase K in deuterated solution for neutron analysis

Chatake, Toshiyuki*; Kurihara, Kazuo; Kuroki, Ryota; Morimoto, Yukio*

Proteinase K (PK) has highly activity in various environments. The aim of our study is to carry out neutron crystallographic analysis of PK for revealing detailed mechanisms of reaction and a resistance to severe environments. As for PK, it is hardly to get large crystals suitable for neutron diffraction study. Moreover, many NO$$_{3}$$ ions locate on the surface of this protein, and some amino acids seemed to be distorted. At first, we found a new crystallization condition. PK crystals have so excellent quality that 1.05 ${AA}$ X-ray diffraction data could be collected using a synchrotron radiation. Next, crystallizations were carried out in the deuterated solution. D$$_{2}$$O solution had a small influence on the crystallization, and this crystallization condition was adequate for neutron experiment. Still photographs of deuterated crystals were collected with 12 hours exposure time using BIX-3 neutron diffractometer at JRR-3. Several diffraction spots could be identified.



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